Photoactive, heterobifunctional cross-linking reagent. Typically, initial reaction couples via ester to primary amine by amide bond formation in the pH range 6.5-8.5. Second bonding occurs during UV irradiation (250-350 nm) via reactive nitrene. The latter bonding is rapid and non-specific.
Przestroga
Reducing agents such as thiols may reduce the azide to amine and should be avoided. Initial manipulations and coupling should be performed under reduced light.
Inne uwagi
Note that the nitro substituent provides an absorption band at a longer wavelength compared to simple aryl azide.
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Rat adipocyte plasma membranes were incubated with the A1 adenosine receptor agonist, 125I-hydroxyphenylisopropyl adenosine (1 nM) and then treated with the photoactive cross-linking agent, ANB-NOS. The membranes were solubilized and analyzed by SDS-PAGE and autoradiography. A single protein, Mr approx.
Phosphorylase kinase, a regulatory enzyme of glycogenolysis in skeletal muscle, is a hexadecameric oligomer consisting of four copies each of a catalytic subunit (gamma) and three regulatory subunits (alpha, beta, and delta, the last being endogenous calmodulin). The enzyme is
The Journal of biological chemistry, 265(14), 8304-8310 (1990-05-15)
Pharmacological studies indicate that peptide YY (PYY) and neuropeptide Y interact with multiple binding sites, categorized as Y1 and Y2 subtypes. In order to identify and structurally characterize the Y1 and Y2 receptors we covalently cross-linked [125I-Tyr36]PYY to its receptors.
Journal of immunology (Baltimore, Md. : 1950), 157(1), 213-220 (1996-07-01)
Cytotoxic T lymphocytes recognize antigenic peptides presented by MHC class I molecules. The peptides are generated in the cytosol by proteasomes, and probably also other proteases, and are then translocated into the endoplasmic reticulum (ER) lumen. The transporters associated with
The Biochemical journal, 235(3), 879-882 (1986-05-01)
We have recently shown that the beta subunit of thyrotropin (TSH) can be cross-linked to the TSH receptor [Buckland, Strickland, Pierce & Rees Smith (1985) Endocrinology (Baltimore) 116, 2122-2124; Buckland, Strickland & Rees Smith (1985) Biochem. Soc. Trans. 13, 942-943].
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